JP6145089B2 - ストロマ細胞由来因子−1のプロテアーゼ耐性変異体を用いた、組織損傷を修復するための方法 - Google Patents
ストロマ細胞由来因子−1のプロテアーゼ耐性変異体を用いた、組織損傷を修復するための方法 Download PDFInfo
- Publication number
- JP6145089B2 JP6145089B2 JP2014514581A JP2014514581A JP6145089B2 JP 6145089 B2 JP6145089 B2 JP 6145089B2 JP 2014514581 A JP2014514581 A JP 2014514581A JP 2014514581 A JP2014514581 A JP 2014514581A JP 6145089 B2 JP6145089 B2 JP 6145089B2
- Authority
- JP
- Japan
- Prior art keywords
- sdf
- pharmaceutical composition
- disease
- msdf
- peptide
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Fee Related
Links
- 108010008951 Chemokine CXCL12 Proteins 0.000 title claims description 190
- 230000000451 tissue damage Effects 0.000 title claims description 64
- 231100000827 tissue damage Toxicity 0.000 title claims description 64
- 102000006573 Chemokine CXCL12 Human genes 0.000 title description 159
- 238000000034 method Methods 0.000 title description 68
- 108091005804 Peptidases Proteins 0.000 title description 22
- 239000004365 Protease Substances 0.000 title description 21
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 title 1
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 127
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 61
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 60
- 235000001014 amino acid Nutrition 0.000 claims description 52
- 201000010099 disease Diseases 0.000 claims description 48
- 150000001413 amino acids Chemical group 0.000 claims description 47
- 239000000203 mixture Substances 0.000 claims description 40
- 238000003745 diagnosis Methods 0.000 claims description 33
- 239000008194 pharmaceutical composition Substances 0.000 claims description 31
- 210000003462 vein Anatomy 0.000 claims description 23
- 208000010125 myocardial infarction Diseases 0.000 claims description 22
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims description 21
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 20
- 208000018262 Peripheral vascular disease Diseases 0.000 claims description 18
- 210000001519 tissue Anatomy 0.000 claims description 18
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 claims description 17
- 102000016622 Dipeptidyl Peptidase 4 Human genes 0.000 claims description 17
- 101000930822 Giardia intestinalis Dipeptidyl-peptidase 4 Proteins 0.000 claims description 17
- 102000001776 Matrix metalloproteinase-9 Human genes 0.000 claims description 17
- 108010015302 Matrix metalloproteinase-9 Proteins 0.000 claims description 17
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims description 16
- 239000004474 valine Substances 0.000 claims description 16
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims description 15
- 206010012601 diabetes mellitus Diseases 0.000 claims description 15
- 125000000962 organic group Chemical group 0.000 claims description 14
- LKDMKWNDBAVNQZ-UHFFFAOYSA-N 4-[[1-[[1-[2-[[1-(4-nitroanilino)-1-oxo-3-phenylpropan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoic acid Chemical compound OC(=O)CCC(=O)NC(C)C(=O)NC(C)C(=O)N1CCCC1C(=O)NC(C(=O)NC=1C=CC(=CC=1)[N+]([O-])=O)CC1=CC=CC=C1 LKDMKWNDBAVNQZ-UHFFFAOYSA-N 0.000 claims description 13
- 102000004173 Cathepsin G Human genes 0.000 claims description 13
- 108090000617 Cathepsin G Proteins 0.000 claims description 13
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 13
- 108010028275 Leukocyte Elastase Proteins 0.000 claims description 13
- 102000016799 Leukocyte elastase Human genes 0.000 claims description 13
- 230000029663 wound healing Effects 0.000 claims description 12
- 235000018417 cysteine Nutrition 0.000 claims description 11
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 11
- 210000001744 T-lymphocyte Anatomy 0.000 claims description 10
- 230000031902 chemoattractant activity Effects 0.000 claims description 10
- 210000005003 heart tissue Anatomy 0.000 claims description 10
- 230000002779 inactivation Effects 0.000 claims description 10
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 9
- 108020001507 fusion proteins Proteins 0.000 claims description 9
- 102000037865 fusion proteins Human genes 0.000 claims description 9
- 230000002093 peripheral effect Effects 0.000 claims description 9
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 claims description 7
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 claims description 7
- 208000024891 symptom Diseases 0.000 claims description 7
- 208000037816 tissue injury Diseases 0.000 claims description 7
- 230000002792 vascular Effects 0.000 claims description 7
- 239000004471 Glycine Substances 0.000 claims description 6
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 6
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 claims description 6
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims description 6
- 239000004473 Threonine Substances 0.000 claims description 6
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 6
- 208000014674 injury Diseases 0.000 claims description 6
- 238000001361 intraarterial administration Methods 0.000 claims description 6
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 claims description 5
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims description 5
- 206010007558 Cardiac failure chronic Diseases 0.000 claims description 4
- 201000002818 limb ischemia Diseases 0.000 claims description 4
- 230000007998 vessel formation Effects 0.000 claims description 4
- 208000024172 Cardiovascular disease Diseases 0.000 claims description 3
- 108060003951 Immunoglobulin Proteins 0.000 claims description 3
- 102000002274 Matrix Metalloproteinases Human genes 0.000 claims description 3
- 108010000684 Matrix Metalloproteinases Proteins 0.000 claims description 3
- 102000018358 immunoglobulin Human genes 0.000 claims description 3
- 230000002829 reductive effect Effects 0.000 claims description 3
- 230000008733 trauma Effects 0.000 claims description 3
- 102100021669 Stromal cell-derived factor 1 Human genes 0.000 claims 13
- 101710088580 Stromal cell-derived factor 1 Proteins 0.000 claims 12
- 102100026802 72 kDa type IV collagenase Human genes 0.000 claims 2
- 101710151806 72 kDa type IV collagenase Proteins 0.000 claims 2
- ONDPHDOFVYQSGI-UHFFFAOYSA-N zinc nitrate Chemical compound [Zn+2].[O-][N+]([O-])=O.[O-][N+]([O-])=O ONDPHDOFVYQSGI-UHFFFAOYSA-N 0.000 claims 1
- 229940024606 amino acid Drugs 0.000 description 43
- 238000001990 intravenous administration Methods 0.000 description 42
- 229920001184 polypeptide Polymers 0.000 description 29
- 102000035195 Peptidases Human genes 0.000 description 21
- 125000003275 alpha amino acid group Chemical group 0.000 description 18
- 102000000424 Matrix Metalloproteinase 2 Human genes 0.000 description 16
- 108010016165 Matrix Metalloproteinase 2 Proteins 0.000 description 16
- 208000027418 Wounds and injury Diseases 0.000 description 16
- 235000019419 proteases Nutrition 0.000 description 14
- 206010052428 Wound Diseases 0.000 description 13
- 208000035475 disorder Diseases 0.000 description 13
- 238000011282 treatment Methods 0.000 description 13
- 230000035772 mutation Effects 0.000 description 11
- 108090000623 proteins and genes Proteins 0.000 description 11
- 241000700159 Rattus Species 0.000 description 9
- 235000018102 proteins Nutrition 0.000 description 9
- 102000004169 proteins and genes Human genes 0.000 description 9
- 102100032936 Carboxypeptidase M Human genes 0.000 description 8
- 108090000007 Carboxypeptidase M Proteins 0.000 description 8
- 108010085169 Lysine carboxypeptidase Proteins 0.000 description 8
- 238000007792 addition Methods 0.000 description 8
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 7
- 239000003814 drug Substances 0.000 description 7
- 238000001802 infusion Methods 0.000 description 7
- 208000030831 Peripheral arterial occlusive disease Diseases 0.000 description 6
- 125000000539 amino acid group Chemical group 0.000 description 6
- 238000003556 assay Methods 0.000 description 6
- 238000003776 cleavage reaction Methods 0.000 description 6
- 230000006378 damage Effects 0.000 description 6
- 230000001965 increasing effect Effects 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 230000008439 repair process Effects 0.000 description 6
- 230000007017 scission Effects 0.000 description 6
- 210000000130 stem cell Anatomy 0.000 description 6
- 230000017423 tissue regeneration Effects 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 5
- 230000000694 effects Effects 0.000 description 5
- 150000007523 nucleic acids Chemical class 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 108700024394 Exon Proteins 0.000 description 4
- AEMRFAOFKBGASW-UHFFFAOYSA-N Glycolic acid Polymers OCC(O)=O AEMRFAOFKBGASW-UHFFFAOYSA-N 0.000 description 4
- 208000005764 Peripheral Arterial Disease Diseases 0.000 description 4
- 108010020346 Polyglutamic Acid Proteins 0.000 description 4
- 229920000954 Polyglycolide Polymers 0.000 description 4
- 208000025865 Ulcer Diseases 0.000 description 4
- 230000033115 angiogenesis Effects 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 239000002975 chemoattractant Substances 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 238000013270 controlled release Methods 0.000 description 4
- 239000003937 drug carrier Substances 0.000 description 4
- 239000012634 fragment Substances 0.000 description 4
- 230000006870 function Effects 0.000 description 4
- 230000000004 hemodynamic effect Effects 0.000 description 4
- 238000004128 high performance liquid chromatography Methods 0.000 description 4
- 108020004707 nucleic acids Proteins 0.000 description 4
- 102000039446 nucleic acids Human genes 0.000 description 4
- 229920000747 poly(lactic acid) Polymers 0.000 description 4
- 229920001606 poly(lactic acid-co-glycolic acid) Polymers 0.000 description 4
- 229920002643 polyglutamic acid Polymers 0.000 description 4
- 230000001737 promoting effect Effects 0.000 description 4
- 238000011084 recovery Methods 0.000 description 4
- 210000005245 right atrium Anatomy 0.000 description 4
- -1 serine amino acid Chemical class 0.000 description 4
- 238000013268 sustained release Methods 0.000 description 4
- 239000012730 sustained-release form Substances 0.000 description 4
- 238000002560 therapeutic procedure Methods 0.000 description 4
- 231100000397 ulcer Toxicity 0.000 description 4
- 210000002620 vena cava superior Anatomy 0.000 description 4
- 102000019034 Chemokines Human genes 0.000 description 3
- 108010012236 Chemokines Proteins 0.000 description 3
- 206010063837 Reperfusion injury Diseases 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 210000001185 bone marrow Anatomy 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 230000003111 delayed effect Effects 0.000 description 3
- 238000002716 delivery method Methods 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 230000035876 healing Effects 0.000 description 3
- 230000004217 heart function Effects 0.000 description 3
- 229910052739 hydrogen Inorganic materials 0.000 description 3
- 239000001257 hydrogen Substances 0.000 description 3
- 230000001976 improved effect Effects 0.000 description 3
- 208000012947 ischemia reperfusion injury Diseases 0.000 description 3
- 210000004731 jugular vein Anatomy 0.000 description 3
- 230000000670 limiting effect Effects 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 125000003729 nucleotide group Chemical group 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 230000010410 reperfusion Effects 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 238000001356 surgical procedure Methods 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 229940124597 therapeutic agent Drugs 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- 230000000472 traumatic effect Effects 0.000 description 3
- 210000001631 vena cava inferior Anatomy 0.000 description 3
- UUUHXMGGBIUAPW-UHFFFAOYSA-N 1-[1-[2-[[5-amino-2-[[1-[5-(diaminomethylideneamino)-2-[[1-[3-(1h-indol-3-yl)-2-[(5-oxopyrrolidine-2-carbonyl)amino]propanoyl]pyrrolidine-2-carbonyl]amino]pentanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-3-methylpentanoyl]pyrrolidine-2-carbon Chemical compound C1CCC(C(=O)N2C(CCC2)C(O)=O)N1C(=O)C(C(C)CC)NC(=O)C(CCC(N)=O)NC(=O)C1CCCN1C(=O)C(CCCN=C(N)N)NC(=O)C1CCCN1C(=O)C(CC=1C2=CC=CC=C2NC=1)NC(=O)C1CCC(=O)N1 UUUHXMGGBIUAPW-UHFFFAOYSA-N 0.000 description 2
- 102100031573 Hematopoietic progenitor cell antigen CD34 Human genes 0.000 description 2
- 101000777663 Homo sapiens Hematopoietic progenitor cell antigen CD34 Proteins 0.000 description 2
- 206010061216 Infarction Diseases 0.000 description 2
- PIWKPBJCKXDKJR-UHFFFAOYSA-N Isoflurane Chemical compound FC(F)OC(Cl)C(F)(F)F PIWKPBJCKXDKJR-UHFFFAOYSA-N 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 102000004270 Peptidyl-Dipeptidase A Human genes 0.000 description 2
- 108090000882 Peptidyl-Dipeptidase A Proteins 0.000 description 2
- 229920001054 Poly(ethylene‐co‐vinyl acetate) Polymers 0.000 description 2
- 229920002845 Poly(methacrylic acid) Polymers 0.000 description 2
- 229920002732 Polyanhydride Polymers 0.000 description 2
- 229920001710 Polyorthoester Polymers 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 229920002125 Sokalan® Polymers 0.000 description 2
- 208000026062 Tissue disease Diseases 0.000 description 2
- RMRJXGBAOAMLHD-IHFGGWKQSA-N buprenorphine Chemical compound C([C@]12[C@H]3OC=4C(O)=CC=C(C2=4)C[C@@H]2[C@]11CC[C@]3([C@H](C1)[C@](C)(O)C(C)(C)C)OC)CN2CC1CC1 RMRJXGBAOAMLHD-IHFGGWKQSA-N 0.000 description 2
- 229960001736 buprenorphine Drugs 0.000 description 2
- 210000004027 cell Anatomy 0.000 description 2
- 230000012292 cell migration Effects 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 230000035605 chemotaxis Effects 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 230000002526 effect on cardiovascular system Effects 0.000 description 2
- 230000002708 enhancing effect Effects 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 230000009067 heart development Effects 0.000 description 2
- 150000002431 hydrogen Chemical class 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 230000007574 infarction Effects 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 238000002642 intravenous therapy Methods 0.000 description 2
- 229960002725 isoflurane Drugs 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 238000010232 migration assay Methods 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 238000010647 peptide synthesis reaction Methods 0.000 description 2
- 239000000816 peptidomimetic Substances 0.000 description 2
- 230000003285 pharmacodynamic effect Effects 0.000 description 2
- 230000026731 phosphorylation Effects 0.000 description 2
- 238000006366 phosphorylation reaction Methods 0.000 description 2
- 229920000191 poly(N-vinyl pyrrolidone) Polymers 0.000 description 2
- 229920001200 poly(ethylene-vinyl acetate) Polymers 0.000 description 2
- 229920003229 poly(methyl methacrylate) Polymers 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 229920002338 polyhydroxyethylmethacrylate Polymers 0.000 description 2
- 239000004926 polymethyl methacrylate Substances 0.000 description 2
- 229920002451 polyvinyl alcohol Polymers 0.000 description 2
- 230000004481 post-translational protein modification Effects 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- AQHHHDLHHXJYJD-UHFFFAOYSA-N propranolol Chemical compound C1=CC=C2C(OCC(O)CNC(C)C)=CC=CC2=C1 AQHHHDLHHXJYJD-UHFFFAOYSA-N 0.000 description 2
- 229930182852 proteinogenic amino acid Natural products 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- LOUPRKONTZGTKE-LHHVKLHASA-N quinidine Chemical compound C([C@H]([C@H](C1)C=C)C2)C[N@@]1[C@H]2[C@@H](O)C1=CC=NC2=CC=C(OC)C=C21 LOUPRKONTZGTKE-LHHVKLHASA-N 0.000 description 2
- 230000008929 regeneration Effects 0.000 description 2
- 238000011069 regeneration method Methods 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 210000002536 stromal cell Anatomy 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 230000002194 synthesizing effect Effects 0.000 description 2
- RMMXLENWKUUMAY-UHFFFAOYSA-N telmisartan Chemical compound CCCC1=NC2=C(C)C=C(C=3N(C4=CC=CC=C4N=3)C)C=C2N1CC(C=C1)=CC=C1C1=CC=CC=C1C(O)=O RMMXLENWKUUMAY-UHFFFAOYSA-N 0.000 description 2
- 238000011191 terminal modification Methods 0.000 description 2
- 238000011269 treatment regimen Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- CEMAWMOMDPGJMB-UHFFFAOYSA-N (+-)-Oxprenolol Chemical compound CC(C)NCC(O)COC1=CC=CC=C1OCC=C CEMAWMOMDPGJMB-UHFFFAOYSA-N 0.000 description 1
- VLPIATFUUWWMKC-SNVBAGLBSA-N (2r)-1-(2,6-dimethylphenoxy)propan-2-amine Chemical compound C[C@@H](N)COC1=C(C)C=CC=C1C VLPIATFUUWWMKC-SNVBAGLBSA-N 0.000 description 1
- BUJAGSGYPOAWEI-SECBINFHSA-N (2r)-2-amino-n-(2,6-dimethylphenyl)propanamide Chemical compound C[C@@H](N)C(=O)NC1=C(C)C=CC=C1C BUJAGSGYPOAWEI-SECBINFHSA-N 0.000 description 1
- BIDNLKIUORFRQP-XYGFDPSESA-N (2s,4s)-4-cyclohexyl-1-[2-[[(1s)-2-methyl-1-propanoyloxypropoxy]-(4-phenylbutyl)phosphoryl]acetyl]pyrrolidine-2-carboxylic acid Chemical compound C([P@@](=O)(O[C@H](OC(=O)CC)C(C)C)CC(=O)N1[C@@H](C[C@H](C1)C1CCCCC1)C(O)=O)CCCC1=CC=CC=C1 BIDNLKIUORFRQP-XYGFDPSESA-N 0.000 description 1
- ZGGHKIMDNBDHJB-NRFPMOEYSA-M (3R,5S)-fluvastatin sodium Chemical compound [Na+].C12=CC=CC=C2N(C(C)C)C(\C=C\[C@@H](O)C[C@@H](O)CC([O-])=O)=C1C1=CC=C(F)C=C1 ZGGHKIMDNBDHJB-NRFPMOEYSA-M 0.000 description 1
- METKIMKYRPQLGS-GFCCVEGCSA-N (R)-atenolol Chemical compound CC(C)NC[C@@H](O)COC1=CC=C(CC(N)=O)C=C1 METKIMKYRPQLGS-GFCCVEGCSA-N 0.000 description 1
- TWBNMYSKRDRHAT-RCWTXCDDSA-N (S)-timolol hemihydrate Chemical compound O.CC(C)(C)NC[C@H](O)COC1=NSN=C1N1CCOCC1.CC(C)(C)NC[C@H](O)COC1=NSN=C1N1CCOCC1 TWBNMYSKRDRHAT-RCWTXCDDSA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- SGTNSNPWRIOYBX-UHFFFAOYSA-N 2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile Chemical compound C1=C(OC)C(OC)=CC=C1CCN(C)CCCC(C#N)(C(C)C)C1=CC=C(OC)C(OC)=C1 SGTNSNPWRIOYBX-UHFFFAOYSA-N 0.000 description 1
- ODHCTXKNWHHXJC-VKHMYHEASA-N 5-oxo-L-proline Chemical compound OC(=O)[C@@H]1CCC(=O)N1 ODHCTXKNWHHXJC-VKHMYHEASA-N 0.000 description 1
- 230000005730 ADP ribosylation Effects 0.000 description 1
- ITPDYQOUSLNIHG-UHFFFAOYSA-N Amiodarone hydrochloride Chemical compound [Cl-].CCCCC=1OC2=CC=CC=C2C=1C(=O)C1=CC(I)=C(OCC[NH+](CC)CC)C(I)=C1 ITPDYQOUSLNIHG-UHFFFAOYSA-N 0.000 description 1
- 102000008873 Angiotensin II receptor Human genes 0.000 description 1
- 108050000824 Angiotensin II receptor Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 102000003916 Arrestin Human genes 0.000 description 1
- 108090000328 Arrestin Proteins 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- BSYNRYMUTXBXSQ-UHFFFAOYSA-N Aspirin Chemical compound CC(=O)OC1=CC=CC=C1C(O)=O BSYNRYMUTXBXSQ-UHFFFAOYSA-N 0.000 description 1
- XUKUURHRXDUEBC-KAYWLYCHSA-N Atorvastatin Chemical compound C=1C=CC=CC=1C1=C(C=2C=CC(F)=CC=2)N(CC[C@@H](O)C[C@@H](O)CC(O)=O)C(C(C)C)=C1C(=O)NC1=CC=CC=C1 XUKUURHRXDUEBC-KAYWLYCHSA-N 0.000 description 1
- XUKUURHRXDUEBC-UHFFFAOYSA-N Atorvastatin Natural products C=1C=CC=CC=1C1=C(C=2C=CC(F)=CC=2)N(CCC(O)CC(O)CC(O)=O)C(C(C)C)=C1C(=O)NC1=CC=CC=C1 XUKUURHRXDUEBC-UHFFFAOYSA-N 0.000 description 1
- 239000005552 B01AC04 - Clopidogrel Substances 0.000 description 1
- 239000005528 B01AC05 - Ticlopidine Substances 0.000 description 1
- 239000005465 B01AC22 - Prasugrel Substances 0.000 description 1
- XPCFTKFZXHTYIP-PMACEKPBSA-N Benazepril Chemical compound C([C@@H](C(=O)OCC)N[C@@H]1C(N(CC(O)=O)C2=CC=CC=C2CC1)=O)CC1=CC=CC=C1 XPCFTKFZXHTYIP-PMACEKPBSA-N 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 239000002083 C09CA01 - Losartan Substances 0.000 description 1
- 239000002080 C09CA02 - Eprosartan Substances 0.000 description 1
- 239000002947 C09CA04 - Irbesartan Substances 0.000 description 1
- 239000002053 C09CA06 - Candesartan Substances 0.000 description 1
- 239000005537 C09CA07 - Telmisartan Substances 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 206010056340 Diabetic ulcer Diseases 0.000 description 1
- 102100025012 Dipeptidyl peptidase 4 Human genes 0.000 description 1
- 108010061435 Enalapril Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 108010056764 Eptifibatide Proteins 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 108091006020 Fc-tagged proteins Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- DJBNUMBKLMJRSA-UHFFFAOYSA-N Flecainide Chemical compound FC(F)(F)COC1=CC=C(OCC(F)(F)F)C(C(=O)NCC2NCCCC2)=C1 DJBNUMBKLMJRSA-UHFFFAOYSA-N 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 description 1
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 1
- 229940121710 HMGCoA reductase inhibitor Drugs 0.000 description 1
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000908391 Homo sapiens Dipeptidyl peptidase 4 Proteins 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- ALOBUEHUHMBRLE-UHFFFAOYSA-N Ibutilide Chemical compound CCCCCCCN(CC)CCCC(O)C1=CC=C(NS(C)(=O)=O)C=C1 ALOBUEHUHMBRLE-UHFFFAOYSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N L-cystine Chemical compound [O-]C(=O)[C@@H]([NH3+])CSSC[C@H]([NH3+])C([O-])=O LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- NNJVILVZKWQKPM-UHFFFAOYSA-N Lidocaine Chemical compound CCN(CC)CC(=O)NC1=C(C)C=CC=C1C NNJVILVZKWQKPM-UHFFFAOYSA-N 0.000 description 1
- 108010007859 Lisinopril Proteins 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- SECXISVLQFMRJM-UHFFFAOYSA-N N-Methylpyrrolidone Chemical compound CN1CCCC1=O SECXISVLQFMRJM-UHFFFAOYSA-N 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 239000005480 Olmesartan Substances 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- CXOFVDLJLONNDW-UHFFFAOYSA-N Phenytoin Chemical compound N1C(=O)NC(=O)C1(C=1C=CC=CC=1)C1=CC=CC=C1 CXOFVDLJLONNDW-UHFFFAOYSA-N 0.000 description 1
- TUZYXOIXSAXUGO-UHFFFAOYSA-N Pravastatin Natural products C1=CC(C)C(CCC(O)CC(O)CC(O)=O)C2C(OC(=O)C(C)CC)CC(O)C=C21 TUZYXOIXSAXUGO-UHFFFAOYSA-N 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 102000016971 Proto-Oncogene Proteins c-kit Human genes 0.000 description 1
- 108010014608 Proto-Oncogene Proteins c-kit Proteins 0.000 description 1
- ODHCTXKNWHHXJC-GSVOUGTGSA-N Pyroglutamic acid Natural products OC(=O)[C@H]1CCC(=O)N1 ODHCTXKNWHHXJC-GSVOUGTGSA-N 0.000 description 1
- RYMZZMVNJRMUDD-UHFFFAOYSA-N SJ000286063 Natural products C12C(OC(=O)C(C)(C)CC)CC(C)C=C2C=CC(C)C1CCC1CC(O)CC(=O)O1 RYMZZMVNJRMUDD-UHFFFAOYSA-N 0.000 description 1
- AJLFOPYRIVGYMJ-UHFFFAOYSA-N SJ000287055 Natural products C12C(OC(=O)C(C)CC)CCC=C2C=CC(C)C1CCC1CC(O)CC(=O)O1 AJLFOPYRIVGYMJ-UHFFFAOYSA-N 0.000 description 1
- 206010072170 Skin wound Diseases 0.000 description 1
- 208000006011 Stroke Diseases 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- VXFJYXUZANRPDJ-WTNASJBWSA-N Trandopril Chemical compound C([C@@H](C(=O)OCC)N[C@@H](C)C(=O)N1[C@@H](C[C@H]2CCCC[C@@H]21)C(O)=O)CC1=CC=CC=C1 VXFJYXUZANRPDJ-WTNASJBWSA-N 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 229960000446 abciximab Drugs 0.000 description 1
- 210000001015 abdomen Anatomy 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 229960001138 acetylsalicylic acid Drugs 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- ODHCTXKNWHHXJC-UHFFFAOYSA-N acide pyroglutamique Natural products OC(=O)C1CCC(=O)N1 ODHCTXKNWHHXJC-UHFFFAOYSA-N 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 230000010933 acylation Effects 0.000 description 1
- 238000005917 acylation reaction Methods 0.000 description 1
- 238000011374 additional therapy Methods 0.000 description 1
- 239000000853 adhesive Substances 0.000 description 1
- 230000001070 adhesive effect Effects 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 230000029936 alkylation Effects 0.000 description 1
- 238000005804 alkylation reaction Methods 0.000 description 1
- 230000001668 ameliorated effect Effects 0.000 description 1
- 230000009435 amidation Effects 0.000 description 1
- 238000007112 amidation reaction Methods 0.000 description 1
- 229960005260 amiodarone Drugs 0.000 description 1
- 230000002491 angiogenic effect Effects 0.000 description 1
- 239000003416 antiarrhythmic agent Substances 0.000 description 1
- 239000002220 antihypertensive agent Substances 0.000 description 1
- 229940127088 antihypertensive drug Drugs 0.000 description 1
- 229940127218 antiplatelet drug Drugs 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 230000010516 arginylation Effects 0.000 description 1
- 238000003491 array Methods 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 229960002274 atenolol Drugs 0.000 description 1
- 229960005370 atorvastatin Drugs 0.000 description 1
- 229960004530 benazepril Drugs 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 239000002876 beta blocker Substances 0.000 description 1
- 229940097320 beta blocking agent Drugs 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 239000013060 biological fluid Substances 0.000 description 1
- 230000006287 biotinylation Effects 0.000 description 1
- 238000007413 biotinylation Methods 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 229960002624 bretylium tosilate Drugs 0.000 description 1
- KVWNWTZZBKCOPM-UHFFFAOYSA-M bretylium tosylate Chemical compound CC1=CC=C(S([O-])(=O)=O)C=C1.CC[N+](C)(C)CC1=CC=CC=C1Br KVWNWTZZBKCOPM-UHFFFAOYSA-M 0.000 description 1
- 229960000932 candesartan Drugs 0.000 description 1
- SGZAIDDFHDDFJU-UHFFFAOYSA-N candesartan Chemical compound CCOC1=NC2=CC=CC(C(O)=O)=C2N1CC(C=C1)=CC=C1C1=CC=CC=C1C1=NN=N[N]1 SGZAIDDFHDDFJU-UHFFFAOYSA-N 0.000 description 1
- 229960000830 captopril Drugs 0.000 description 1
- FAKRSMQSSFJEIM-RQJHMYQMSA-N captopril Chemical compound SC[C@@H](C)C(=O)N1CCC[C@H]1C(O)=O FAKRSMQSSFJEIM-RQJHMYQMSA-N 0.000 description 1
- 230000021235 carbamoylation Effects 0.000 description 1
- 210000001054 cardiac fibroblast Anatomy 0.000 description 1
- 230000007211 cardiovascular event Effects 0.000 description 1
- 210000001715 carotid artery Anatomy 0.000 description 1
- 239000012876 carrier material Substances 0.000 description 1
- 238000002659 cell therapy Methods 0.000 description 1
- 229960005110 cerivastatin Drugs 0.000 description 1
- SEERZIQQUAZTOL-ANMDKAQQSA-N cerivastatin Chemical compound COCC1=C(C(C)C)N=C(C(C)C)C(\C=C\[C@@H](O)C[C@@H](O)CC(O)=O)=C1C1=CC=C(F)C=C1 SEERZIQQUAZTOL-ANMDKAQQSA-N 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 229960004588 cilostazol Drugs 0.000 description 1
- RRGUKTPIGVIEKM-UHFFFAOYSA-N cilostazol Chemical compound C=1C=C2NC(=O)CCC2=CC=1OCCCCC1=NN=NN1C1CCCCC1 RRGUKTPIGVIEKM-UHFFFAOYSA-N 0.000 description 1
- LOUPRKONTZGTKE-UHFFFAOYSA-N cinchonine Natural products C1C(C(C2)C=C)CCN2C1C(O)C1=CC=NC2=CC=C(OC)C=C21 LOUPRKONTZGTKE-UHFFFAOYSA-N 0.000 description 1
- 229960003009 clopidogrel Drugs 0.000 description 1
- GKTWGGQPFAXNFI-HNNXBMFYSA-N clopidogrel Chemical compound C1([C@H](N2CC=3C=CSC=3CC2)C(=O)OC)=CC=CC=C1Cl GKTWGGQPFAXNFI-HNNXBMFYSA-N 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 238000002591 computed tomography Methods 0.000 description 1
- 239000000599 controlled substance Substances 0.000 description 1
- 210000004351 coronary vessel Anatomy 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 229960003067 cystine Drugs 0.000 description 1
- 230000002380 cytological effect Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 230000001934 delay Effects 0.000 description 1
- 230000017858 demethylation Effects 0.000 description 1
- 238000010520 demethylation reaction Methods 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 230000035487 diastolic blood pressure Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 229960004166 diltiazem Drugs 0.000 description 1
- HSUGRBWQSSZJOP-RTWAWAEBSA-N diltiazem Chemical compound C1=CC(OC)=CC=C1[C@H]1[C@@H](OC(C)=O)C(=O)N(CCN(C)C)C2=CC=CC=C2S1 HSUGRBWQSSZJOP-RTWAWAEBSA-N 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 229960002768 dipyridamole Drugs 0.000 description 1
- IZEKFCXSFNUWAM-UHFFFAOYSA-N dipyridamole Chemical compound C=12N=C(N(CCO)CCO)N=C(N3CCCCC3)C2=NC(N(CCO)CCO)=NC=1N1CCCCC1 IZEKFCXSFNUWAM-UHFFFAOYSA-N 0.000 description 1
- UVTNFZQICZKOEM-UHFFFAOYSA-N disopyramide Chemical compound C=1C=CC=NC=1C(C(N)=O)(CCN(C(C)C)C(C)C)C1=CC=CC=C1 UVTNFZQICZKOEM-UHFFFAOYSA-N 0.000 description 1
- 229960001066 disopyramide Drugs 0.000 description 1
- 239000002934 diuretic Substances 0.000 description 1
- 229940030606 diuretics Drugs 0.000 description 1
- 229960002994 dofetilide Drugs 0.000 description 1
- IXTMWRCNAAVVAI-UHFFFAOYSA-N dofetilide Chemical compound C=1C=C(NS(C)(=O)=O)C=CC=1CCN(C)CCOC1=CC=C(NS(C)(=O)=O)C=C1 IXTMWRCNAAVVAI-UHFFFAOYSA-N 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 229940126534 drug product Drugs 0.000 description 1
- 230000013020 embryo development Effects 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 229960000873 enalapril Drugs 0.000 description 1
- GBXSMTUPTTWBMN-XIRDDKMYSA-N enalapril Chemical compound C([C@@H](C(=O)OCC)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(O)=O)CC1=CC=CC=C1 GBXSMTUPTTWBMN-XIRDDKMYSA-N 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 229960004563 eprosartan Drugs 0.000 description 1
- OROAFUQRIXKEMV-LDADJPATSA-N eprosartan Chemical compound C=1C=C(C(O)=O)C=CC=1CN1C(CCCC)=NC=C1\C=C(C(O)=O)/CC1=CC=CS1 OROAFUQRIXKEMV-LDADJPATSA-N 0.000 description 1
- 229960004468 eptifibatide Drugs 0.000 description 1
- GLGOPUHVAZCPRB-LROMGURASA-N eptifibatide Chemical compound N1C(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H](CCCCNC(=N)N)NC(=O)CCSSC[C@@H](C(N)=O)NC(=O)[C@@H]2CCCN2C(=O)[C@@H]1CC1=CN=C2[C]1C=CC=C2 GLGOPUHVAZCPRB-LROMGURASA-N 0.000 description 1
- 230000032050 esterification Effects 0.000 description 1
- 238000005886 esterification reaction Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 210000003191 femoral vein Anatomy 0.000 description 1
- 229960000449 flecainide Drugs 0.000 description 1
- 229920002457 flexible plastic Polymers 0.000 description 1
- 229960003765 fluvastatin Drugs 0.000 description 1
- 238000005755 formation reaction Methods 0.000 description 1
- 230000022244 formylation Effects 0.000 description 1
- 238000006170 formylation reaction Methods 0.000 description 1
- 229960002490 fosinopril Drugs 0.000 description 1
- 230000006251 gamma-carboxylation Effects 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 150000003278 haem Chemical group 0.000 description 1
- 229910052736 halogen Inorganic materials 0.000 description 1
- 150000002367 halogens Chemical class 0.000 description 1
- 210000003958 hematopoietic stem cell Anatomy 0.000 description 1
- 230000017323 hematopoietic stem cell migration to bone marrow Effects 0.000 description 1
- 230000011132 hemopoiesis Effects 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 230000033444 hydroxylation Effects 0.000 description 1
- 238000005805 hydroxylation reaction Methods 0.000 description 1
- 239000002471 hydroxymethylglutaryl coenzyme A reductase inhibitor Substances 0.000 description 1
- 229960004053 ibutilide Drugs 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 238000005462 in vivo assay Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 208000027866 inflammatory disease Diseases 0.000 description 1
- 230000002757 inflammatory effect Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007914 intraventricular administration Methods 0.000 description 1
- PNDPGZBMCMUPRI-UHFFFAOYSA-N iodine Chemical compound II PNDPGZBMCMUPRI-UHFFFAOYSA-N 0.000 description 1
- 229960002198 irbesartan Drugs 0.000 description 1
- YCPOHTHPUREGFM-UHFFFAOYSA-N irbesartan Chemical compound O=C1N(CC=2C=CC(=CC=2)C=2C(=CC=CC=2)C=2[N]N=NN=2)C(CCCC)=NC21CCCC2 YCPOHTHPUREGFM-UHFFFAOYSA-N 0.000 description 1
- 208000028867 ischemia Diseases 0.000 description 1
- 208000023589 ischemic disease Diseases 0.000 description 1
- 230000000302 ischemic effect Effects 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- 210000005240 left ventricle Anatomy 0.000 description 1
- 230000003902 lesion Effects 0.000 description 1
- 229960004194 lidocaine Drugs 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 229960002394 lisinopril Drugs 0.000 description 1
- RLAWWYSOJDYHDC-BZSNNMDCSA-N lisinopril Chemical compound C([C@H](N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(O)=O)C(O)=O)CC1=CC=CC=C1 RLAWWYSOJDYHDC-BZSNNMDCSA-N 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 229960004773 losartan Drugs 0.000 description 1
- KJJZZJSZUJXYEA-UHFFFAOYSA-N losartan Chemical compound CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C=2[N]N=NN=2)C=C1 KJJZZJSZUJXYEA-UHFFFAOYSA-N 0.000 description 1
- 238000002595 magnetic resonance imaging Methods 0.000 description 1
- 238000005399 mechanical ventilation Methods 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 229960002237 metoprolol Drugs 0.000 description 1
- IUBSYMUCCVWXPE-UHFFFAOYSA-N metoprolol Chemical compound COCCC1=CC=C(OCC(O)CNC(C)C)C=C1 IUBSYMUCCVWXPE-UHFFFAOYSA-N 0.000 description 1
- 229950009116 mevastatin Drugs 0.000 description 1
- AJLFOPYRIVGYMJ-INTXDZFKSA-N mevastatin Chemical compound C([C@H]1[C@@H](C)C=CC2=CCC[C@@H]([C@H]12)OC(=O)[C@@H](C)CC)C[C@@H]1C[C@@H](O)CC(=O)O1 AJLFOPYRIVGYMJ-INTXDZFKSA-N 0.000 description 1
- BOZILQFLQYBIIY-UHFFFAOYSA-N mevastatin hydroxy acid Natural products C1=CC(C)C(CCC(O)CC(O)CC(O)=O)C2C(OC(=O)C(C)CC)CCC=C21 BOZILQFLQYBIIY-UHFFFAOYSA-N 0.000 description 1
- 229960003404 mexiletine Drugs 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 230000002107 myocardial effect Effects 0.000 description 1
- 208000031225 myocardial ischemia Diseases 0.000 description 1
- 230000007498 myristoylation Effects 0.000 description 1
- 229960004255 nadolol Drugs 0.000 description 1
- VWPOSFSPZNDTMJ-UCWKZMIHSA-N nadolol Chemical compound C1[C@@H](O)[C@@H](O)CC2=C1C=CC=C2OCC(O)CNC(C)(C)C VWPOSFSPZNDTMJ-UCWKZMIHSA-N 0.000 description 1
- 229960005117 olmesartan Drugs 0.000 description 1
- VTRAEEWXHOVJFV-UHFFFAOYSA-N olmesartan Chemical compound CCCC1=NC(C(C)(C)O)=C(C(O)=O)N1CC1=CC=C(C=2C(=CC=CC=2)C=2NN=NN=2)C=C1 VTRAEEWXHOVJFV-UHFFFAOYSA-N 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 229960004570 oxprenolol Drugs 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000006320 pegylation Effects 0.000 description 1
- 229960002582 perindopril Drugs 0.000 description 1
- IPVQLZZIHOAWMC-QXKUPLGCSA-N perindopril Chemical compound C1CCC[C@H]2C[C@@H](C(O)=O)N(C(=O)[C@H](C)N[C@@H](CCC)C(=O)OCC)[C@H]21 IPVQLZZIHOAWMC-QXKUPLGCSA-N 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 230000002974 pharmacogenomic effect Effects 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 229960002036 phenytoin Drugs 0.000 description 1
- 150000003905 phosphatidylinositols Chemical class 0.000 description 1
- 229960002508 pindolol Drugs 0.000 description 1
- PHUTUTUABXHXLW-UHFFFAOYSA-N pindolol Chemical compound CC(C)NCC(O)COC1=CC=CC2=NC=C[C]12 PHUTUTUABXHXLW-UHFFFAOYSA-N 0.000 description 1
- 229960002797 pitavastatin Drugs 0.000 description 1
- VGYFMXBACGZSIL-MCBHFWOFSA-N pitavastatin Chemical compound OC(=O)C[C@H](O)C[C@H](O)\C=C\C1=C(C2CC2)N=C2C=CC=CC2=C1C1=CC=C(F)C=C1 VGYFMXBACGZSIL-MCBHFWOFSA-N 0.000 description 1
- 229940096701 plain lipid modifying drug hmg coa reductase inhibitors Drugs 0.000 description 1
- 239000000106 platelet aggregation inhibitor Substances 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 229960004197 prasugrel Drugs 0.000 description 1
- DTGLZDAWLRGWQN-UHFFFAOYSA-N prasugrel Chemical compound C1CC=2SC(OC(=O)C)=CC=2CN1C(C=1C(=CC=CC=1)F)C(=O)C1CC1 DTGLZDAWLRGWQN-UHFFFAOYSA-N 0.000 description 1
- 229960002965 pravastatin Drugs 0.000 description 1
- TUZYXOIXSAXUGO-PZAWKZKUSA-N pravastatin Chemical compound C1=C[C@H](C)[C@H](CC[C@@H](O)C[C@@H](O)CC(O)=O)[C@H]2[C@@H](OC(=O)[C@@H](C)CC)C[C@H](O)C=C21 TUZYXOIXSAXUGO-PZAWKZKUSA-N 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000002028 premature Effects 0.000 description 1
- 230000013823 prenylation Effects 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- REQCZEXYDRLIBE-UHFFFAOYSA-N procainamide Chemical compound CCN(CC)CCNC(=O)C1=CC=C(N)C=C1 REQCZEXYDRLIBE-UHFFFAOYSA-N 0.000 description 1
- 229960000244 procainamide Drugs 0.000 description 1
- 229960003712 propranolol Drugs 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 229960001455 quinapril Drugs 0.000 description 1
- JSDRRTOADPPCHY-HSQYWUDLSA-N quinapril Chemical compound C([C@@H](C(=O)OCC)N[C@@H](C)C(=O)N1[C@@H](CC2=CC=CC=C2C1)C(O)=O)CC1=CC=CC=C1 JSDRRTOADPPCHY-HSQYWUDLSA-N 0.000 description 1
- 229960001404 quinidine Drugs 0.000 description 1
- 230000006340 racemization Effects 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 229960003401 ramipril Drugs 0.000 description 1
- HDACQVRGBOVJII-JBDAPHQKSA-N ramipril Chemical compound C([C@@H](C(=O)OCC)N[C@@H](C)C(=O)N1[C@@H](C[C@@H]2CCC[C@@H]21)C(O)=O)CC1=CC=CC=C1 HDACQVRGBOVJII-JBDAPHQKSA-N 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 230000000284 resting effect Effects 0.000 description 1
- 230000000250 revascularization Effects 0.000 description 1
- 238000007363 ring formation reaction Methods 0.000 description 1
- 238000011808 rodent model Methods 0.000 description 1
- 229960000672 rosuvastatin Drugs 0.000 description 1
- BPRHUIZQVSMCRT-VEUZHWNKSA-N rosuvastatin Chemical compound CC(C)C1=NC(N(C)S(C)(=O)=O)=NC(C=2C=CC(F)=CC=2)=C1\C=C\[C@@H](O)C[C@@H](O)CC(O)=O BPRHUIZQVSMCRT-VEUZHWNKSA-N 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 229910052710 silicon Inorganic materials 0.000 description 1
- 239000010703 silicon Substances 0.000 description 1
- 229920002379 silicone rubber Polymers 0.000 description 1
- 239000004945 silicone rubber Substances 0.000 description 1
- 229960002855 simvastatin Drugs 0.000 description 1
- RYMZZMVNJRMUDD-HGQWONQESA-N simvastatin Chemical compound C([C@H]1[C@@H](C)C=CC2=C[C@H](C)C[C@@H]([C@H]12)OC(=O)C(C)(C)CC)C[C@@H]1C[C@@H](O)CC(=O)O1 RYMZZMVNJRMUDD-HGQWONQESA-N 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 229960002370 sotalol Drugs 0.000 description 1
- ZBMZVLHSJCTVON-UHFFFAOYSA-N sotalol Chemical compound CC(C)NCC(O)C1=CC=C(NS(C)(=O)=O)C=C1 ZBMZVLHSJCTVON-UHFFFAOYSA-N 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 238000011476 stem cell transplantation Methods 0.000 description 1
- 230000019635 sulfation Effects 0.000 description 1
- 238000005670 sulfation reaction Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 230000035488 systolic blood pressure Effects 0.000 description 1
- 229960005187 telmisartan Drugs 0.000 description 1
- 125000005931 tert-butyloxycarbonyl group Chemical group [H]C([H])([H])C(OC(*)=O)(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 229960005001 ticlopidine Drugs 0.000 description 1
- PHWBOXQYWZNQIN-UHFFFAOYSA-N ticlopidine Chemical compound ClC1=CC=CC=C1CN1CC(C=CS2)=C2CC1 PHWBOXQYWZNQIN-UHFFFAOYSA-N 0.000 description 1
- 229960004605 timolol Drugs 0.000 description 1
- 229960003425 tirofiban Drugs 0.000 description 1
- COKMIXFXJJXBQG-NRFANRHFSA-N tirofiban Chemical compound C1=CC(C[C@H](NS(=O)(=O)CCCC)C(O)=O)=CC=C1OCCCCC1CCNCC1 COKMIXFXJJXBQG-NRFANRHFSA-N 0.000 description 1
- 229960002872 tocainide Drugs 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 238000002627 tracheal intubation Methods 0.000 description 1
- 229960002051 trandolapril Drugs 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 238000010798 ubiquitination Methods 0.000 description 1
- 230000034512 ubiquitination Effects 0.000 description 1
- 230000002861 ventricular Effects 0.000 description 1
- 210000000596 ventricular septum Anatomy 0.000 description 1
- 229960001722 verapamil Drugs 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/521—Chemokines
- C07K14/522—Alpha-chemokines, e.g. NAP-2, ENA-78, GRO-alpha/MGSA/NAP-3, GRO-beta/MIP-2alpha, GRO-gamma/MIP-2beta, IP-10, GCP-2, MIG, PBSF, PF-4, KC
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/19—Cytokines; Lymphokines; Interferons
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/04—Inotropic agents, i.e. stimulants of cardiac contraction; Drugs for heart failure
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Zoology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Cardiology (AREA)
- Heart & Thoracic Surgery (AREA)
- Diabetes (AREA)
- Toxicology (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Epidemiology (AREA)
- Immunology (AREA)
- Emergency Medicine (AREA)
- Urology & Nephrology (AREA)
- Hematology (AREA)
- Vascular Medicine (AREA)
- Endocrinology (AREA)
- Dermatology (AREA)
- Hospice & Palliative Care (AREA)
- Obesity (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201161494079P | 2011-06-07 | 2011-06-07 | |
| US61/494,079 | 2011-06-07 | ||
| PCT/US2012/041054 WO2012170495A1 (en) | 2011-06-07 | 2012-06-06 | Methods for repairing tissue damage using protease-resistant mutants of stromal cell derived factor-1 |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2017013060A Division JP2017114867A (ja) | 2011-06-07 | 2017-01-27 | ストロマ細胞由来因子−1のプロテアーゼ耐性変異体を用いた、組織損傷を修復するための方法 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2014519514A JP2014519514A (ja) | 2014-08-14 |
| JP2014519514A5 JP2014519514A5 (enExample) | 2015-04-02 |
| JP6145089B2 true JP6145089B2 (ja) | 2017-06-07 |
Family
ID=47296407
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2014514581A Expired - Fee Related JP6145089B2 (ja) | 2011-06-07 | 2012-06-06 | ストロマ細胞由来因子−1のプロテアーゼ耐性変異体を用いた、組織損傷を修復するための方法 |
| JP2017013060A Pending JP2017114867A (ja) | 2011-06-07 | 2017-01-27 | ストロマ細胞由来因子−1のプロテアーゼ耐性変異体を用いた、組織損傷を修復するための方法 |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2017013060A Pending JP2017114867A (ja) | 2011-06-07 | 2017-01-27 | ストロマ細胞由来因子−1のプロテアーゼ耐性変異体を用いた、組織損傷を修復するための方法 |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US10662234B2 (enExample) |
| EP (1) | EP2717894B1 (enExample) |
| JP (2) | JP6145089B2 (enExample) |
| CN (1) | CN103747795A (enExample) |
| AU (2) | AU2012268078B2 (enExample) |
| CA (1) | CA2838155C (enExample) |
| IL (1) | IL229697A0 (enExample) |
| WO (1) | WO2012170495A1 (enExample) |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2011106234A1 (en) | 2010-02-25 | 2011-09-01 | Provasculon, Inc. | Protease-resistant mutants of stromal cell derived factor-1 in the repair of tissue damage |
| JP6145089B2 (ja) | 2011-06-07 | 2017-06-07 | メソブラスト インターナショナル エスエイアールエル | ストロマ細胞由来因子−1のプロテアーゼ耐性変異体を用いた、組織損傷を修復するための方法 |
| US20160303197A1 (en) * | 2013-12-13 | 2016-10-20 | Mesoblast International Sarl | Methods for repairing tissue damage using protease-resistant mutants of stromal cell derived factor-1 |
| JP6532141B2 (ja) * | 2014-09-26 | 2019-06-19 | ヘリックスミス カンパニー リミテッド | 肝細胞増殖因子及びストローマ細胞由来因子1αを用いた末梢動脈疾患の予防または治療用組成物 |
| CN114366806A (zh) * | 2021-12-16 | 2022-04-19 | 天津市泌尿外科研究所 | 一种纳米黑磷负载sdf-1的纳米药物复合体及其制备方法和应用 |
Family Cites Families (63)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5171680A (en) | 1988-06-14 | 1992-12-15 | Chiron Corporation | Superoxide dismutase analogs having novel binding properties |
| WO1993010261A1 (en) | 1991-11-13 | 1993-05-27 | Dahlbaeck Bjoern | Method for the diagnosis of blood coagulation disorders |
| US5670483A (en) | 1992-12-28 | 1997-09-23 | Massachusetts Insititute Of Technology | Stable macroscopic membranes formed by self-assembly of amphiphilic peptides and uses therefor |
| CA2117953C (en) | 1993-10-14 | 2001-12-11 | Tasuku Honjo | Human stromal derived factor 1 alpha and 1 beta and dnas encoding the same |
| US6100387A (en) | 1997-02-28 | 2000-08-08 | Genetics Institute, Inc. | Chimeric polypeptides containing chemokine domains |
| US6852508B1 (en) | 1997-02-28 | 2005-02-08 | Genetics Institute, Llc | Chemokine with amino-terminal modifications |
| US6214540B1 (en) | 1997-03-26 | 2001-04-10 | University Of Maryland Biotechnology Institute | Chemokines that inhibit immunodeficiency virus infection and methods based thereon |
| CA2305787A1 (en) | 2000-05-09 | 2001-11-09 | The University Of British Columbia | Cxcr4 antagonist treatment of hematopoietic cells |
| JP2002506830A (ja) | 1998-03-13 | 2002-03-05 | ザ ユニバーシティ オブ ブリティッシュ コロンビア | 治療的ケモカイン受容体アンタゴニスト |
| CA2245224A1 (en) | 1998-08-14 | 2000-02-14 | Jiang-Hong Giong | Chemokine receptor antagonists and chemotherapeutics |
| US20020107195A1 (en) | 1998-07-21 | 2002-08-08 | Smithkline Beecham Corporation | Method for inducing chemotaxis in endothelial cells by administering stromal cell derived factor-1alpha |
| US6440934B1 (en) * | 1998-10-13 | 2002-08-27 | Chiron Corporation | Angiogenically effective unit dose of FGF-2 and method of use |
| WO2000023472A2 (en) * | 1998-10-16 | 2000-04-27 | Biogen, Inc. | Interferon-beta fusion proteins and uses |
| US6221856B1 (en) | 1999-02-03 | 2001-04-24 | Inologic, Inc. | Inositol derivatives for inhibiting superoxide anion production |
| AU2003901668A0 (en) | 2003-03-28 | 2003-05-01 | Medvet Science Pty. Ltd. | Non-haemopoietic precursor cells |
| US7368425B2 (en) | 2006-03-24 | 2008-05-06 | Chemokine Therapeutics Corp. | Cyclic peptides for modulating growth of neo-vessels and their use in therapeutic angiogenesis |
| US20050059584A1 (en) | 2002-08-16 | 2005-03-17 | Ahmed Merzouk | Novel chemokine mimetics synthesis and their use |
| CA2335109A1 (en) | 2000-04-12 | 2001-10-12 | Chemokine Therapeutics Corporation | Cxcr4 agonist treatment of hematopoietic cells |
| US7378098B2 (en) | 2000-04-12 | 2008-05-27 | The University Of British Columbia | CXC chemokine receptor 4 agonist peptides |
| DE10027383A1 (de) | 2000-06-02 | 2001-12-20 | Rhein Biotech Proz & Prod Gmbh | Nukleinsäure-Molekül umfassend eine für ein Chemokin, einen Neuropeptid-Präkursor oder mindestens ein Neuropeptid kodierende Nukleinsäuresequenz |
| CA2412436C (en) | 2000-06-05 | 2013-05-21 | The Trustees Of Columbia University In The City Of New York | Identification and use of human bone marrow-derived endothelial progenitor cells to improve myocardial function after ischemic injury |
| US7547674B2 (en) | 2001-06-06 | 2009-06-16 | New York Medical College | Methods and compositions for the repair and/or regeneration of damaged myocardium |
| AU2002235168A1 (en) | 2000-11-05 | 2002-05-15 | University Of Florida | Targeting pluripotent stem cells to tissues |
| WO2002038172A2 (en) | 2000-11-09 | 2002-05-16 | Genetics Institute, Llc | Sdf-1 beta expressing tumor cells as tumor vaccines |
| WO2002043758A2 (en) | 2000-12-01 | 2002-06-06 | Schering Corporation | Uses of mammalian genes and related reagents |
| AU2002235175A1 (en) | 2000-12-06 | 2002-06-18 | Tularik, Inc. | Lometrexol combination therapy |
| AU2002348241A1 (en) | 2001-11-24 | 2003-06-10 | Image Analysis, Inc. | Automatic detection and quantification of coronary and aortic calcium |
| US20030199464A1 (en) | 2002-04-23 | 2003-10-23 | Silviu Itescu | Regeneration of endogenous myocardial tissue by induction of neovascularization |
| US7485141B2 (en) | 2002-05-10 | 2009-02-03 | Cordis Corporation | Method of placing a tubular membrane on a structural frame |
| US20050142101A1 (en) | 2002-05-10 | 2005-06-30 | Ulf Forssmann | Method of inhibiting the emigration of cells from the intravascular compartment into tissues |
| US20050065064A1 (en) | 2002-08-09 | 2005-03-24 | Elias Lolis | Identification of allosteric peptide agonists of CXCR4 |
| WO2008121719A1 (en) | 2007-03-30 | 2008-10-09 | The Cleveland Clinic Foundation | Method of treating ischemic disorders |
| US20040037811A1 (en) | 2002-08-22 | 2004-02-26 | The Cleveland Clinic Foundation | Stromal cell-derived factor-1 mediates stem cell homing and tissue regeneration in ischemic cardiomyopathy |
| US20050271639A1 (en) | 2002-08-22 | 2005-12-08 | Penn Marc S | Genetically engineered cells for therapeutic applications |
| WO2004017909A2 (en) | 2002-08-23 | 2004-03-04 | Bristol-Myers Squibb Company | Methods of reducing ischemic injury |
| US20070060512A1 (en) | 2003-03-04 | 2007-03-15 | Homayoun Sadeghi | Dipeptidyl-peptidase protected protein |
| WO2004094465A2 (en) | 2003-04-23 | 2004-11-04 | The Board Of Trustees Of The University Of Illinois Office Of Technology Management University Of Illinois At Urbana-Champaign | Synthetic molecules that mimic chemokines |
| WO2006124013A2 (en) | 2004-04-30 | 2006-11-23 | Five Prime Therapeutics, Inc. | Novel stromal cell-derived factor-1 polypeptides, polynucleotides, modulators thereof, and method of use |
| US20090285785A1 (en) | 2004-09-17 | 2009-11-19 | Cellgentech, Inc. | External Agent for Treatment of Skin Ulcer |
| KR101598947B1 (ko) | 2004-09-24 | 2016-03-08 | 메소블라스트, 아이엔씨. | 간엽 전구세포의 증식 및/또는 생존성 증강 방법 |
| WO2006047315A2 (en) | 2004-10-25 | 2006-05-04 | The Brigham And Women's Hospital, Inc. | Targeted delivery of biological factors using self-assembling peptide nanofibers |
| US20060110374A1 (en) | 2004-11-24 | 2006-05-25 | Dudy Czeiger | Method to accelerate stem cell recruitment and homing |
| US7429567B2 (en) | 2005-01-04 | 2008-09-30 | The Brigham And Women's Hospital, Inc. | Sustained delivery of PDGF using self-assembling peptide nanofibers |
| US8153592B2 (en) | 2005-01-10 | 2012-04-10 | Mayo Foundation For Medical Education And Research | Modulating toll-like receptor activity |
| EP1879606B1 (en) | 2005-04-25 | 2013-06-12 | Massachusetts Institute of Technology | Self-assembling peptides for promoting hemostasis |
| WO2007051785A2 (en) * | 2005-10-31 | 2007-05-10 | Laboratoire Serono S.A. | Use of sdf-1 for the treatment and/or prevention of neurological diseases |
| WO2007079460A2 (en) | 2006-01-04 | 2007-07-12 | Chemokine Therapeutics Corporation | Design of cxc chemokine analogs for the treatment of human diseases |
| US7776816B2 (en) | 2006-01-20 | 2010-08-17 | Board Of Regents, The University Of Texas System | Preserving hypoxic tissue |
| WO2008018641A1 (en) | 2006-08-11 | 2008-02-14 | Ono Pharmaceutical Co., Ltd. | Monoclonal antibodies against stromal derived factor-1 (sdf-1) |
| US7696309B2 (en) | 2006-10-23 | 2010-04-13 | The Brigham And Women's Hospital, Inc. | Protease resistant mutants of stromal cell derived factor-1 in the repair of tissue damage |
| US20080194478A1 (en) | 2007-02-09 | 2008-08-14 | Gene Signal International Sa | Wound healing agent and composition |
| ES2325715B1 (es) | 2007-08-03 | 2010-06-17 | Genetrix, S.L. | Poblacion de celulas madre adultas derivadas de tejido adiposo cardiaco y su uso en regeneracion cardiaca. |
| EP2210622B1 (en) | 2007-10-10 | 2015-07-08 | Kyoto University | Therapeutic agent for heart disease, which is intended to be used in cell transplantation therapy |
| EP2218459B1 (en) * | 2007-11-07 | 2012-02-01 | Ono Pharmaceutical Co., Ltd. | Sustained release composition containing sdf-1 |
| EP2100954A1 (en) | 2008-03-10 | 2009-09-16 | Assistance Publique - Hopitaux de Paris | Method for generating primate cardiac progenitor cells for clinical use from primate embryonic stem cells, and their applications |
| WO2010024300A1 (ja) | 2008-08-26 | 2010-03-04 | 国立大学法人 北海道大学 | 骨充填型軟骨組織再生誘導剤 |
| US9072765B2 (en) | 2009-05-20 | 2015-07-07 | Board Of Regents, The University Of Texas System | Identification of micro-RNAs involved in post-myocardial infarction remodeling and heart failure |
| WO2010138180A2 (en) * | 2009-05-26 | 2010-12-02 | The University Of Vermont And State Agriculture College | Compositions and methods for cardiac tissue repair |
| WO2011106234A1 (en) | 2010-02-25 | 2011-09-01 | Provasculon, Inc. | Protease-resistant mutants of stromal cell derived factor-1 in the repair of tissue damage |
| WO2012027170A1 (en) | 2010-08-23 | 2012-03-01 | Provasculon, Inc. | Methods for repairing tissue damage using protease-resistant mutants of stromal cell derived factor-1 |
| EP2610752B1 (en) * | 2010-08-27 | 2017-09-27 | Fujitsu Limited | Parallel computer, job information acquisition program of parallel computer, and job information acquisition method for parallel computer |
| JP6145089B2 (ja) | 2011-06-07 | 2017-06-07 | メソブラスト インターナショナル エスエイアールエル | ストロマ細胞由来因子−1のプロテアーゼ耐性変異体を用いた、組織損傷を修復するための方法 |
| US20160303197A1 (en) | 2013-12-13 | 2016-10-20 | Mesoblast International Sarl | Methods for repairing tissue damage using protease-resistant mutants of stromal cell derived factor-1 |
-
2012
- 2012-06-06 JP JP2014514581A patent/JP6145089B2/ja not_active Expired - Fee Related
- 2012-06-06 EP EP12796309.8A patent/EP2717894B1/en not_active Not-in-force
- 2012-06-06 AU AU2012268078A patent/AU2012268078B2/en not_active Ceased
- 2012-06-06 CN CN201280037907.4A patent/CN103747795A/zh active Pending
- 2012-06-06 CA CA2838155A patent/CA2838155C/en active Active
- 2012-06-06 US US14/124,187 patent/US10662234B2/en not_active Expired - Fee Related
- 2012-06-06 WO PCT/US2012/041054 patent/WO2012170495A1/en not_active Ceased
-
2013
- 2013-11-28 IL IL229697A patent/IL229697A0/en unknown
-
2017
- 2017-01-27 JP JP2017013060A patent/JP2017114867A/ja active Pending
- 2017-08-08 AU AU2017213440A patent/AU2017213440A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| JP2014519514A (ja) | 2014-08-14 |
| IL229697A0 (en) | 2014-01-30 |
| EP2717894B1 (en) | 2018-01-24 |
| AU2012268078B2 (en) | 2017-06-01 |
| EP2717894A4 (en) | 2015-02-25 |
| US20140199304A1 (en) | 2014-07-17 |
| AU2017213440A1 (en) | 2017-08-24 |
| AU2012268078A1 (en) | 2013-12-19 |
| CA2838155A1 (en) | 2012-12-13 |
| US10662234B2 (en) | 2020-05-26 |
| JP2017114867A (ja) | 2017-06-29 |
| WO2012170495A1 (en) | 2012-12-13 |
| CA2838155C (en) | 2021-10-19 |
| CN103747795A (zh) | 2014-04-23 |
| EP2717894A1 (en) | 2014-04-16 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2268710T3 (es) | Uso de los dipeptidos glu-trp para la elaboracion de un medicamento para el tratamiento de diferentes condiciones que involucran neovasculacion. | |
| JP6825181B2 (ja) | 膵炎を治療するための薬剤の製造におけるil−22二量体の使用 | |
| JP2017114867A (ja) | ストロマ細胞由来因子−1のプロテアーゼ耐性変異体を用いた、組織損傷を修復するための方法 | |
| EP2522676A2 (en) | Disintegrin variants and pharmaceutical uses thereof | |
| US20250019677A1 (en) | Methods of improving cardiovascular function and treating cardiovascular disease using a recombinant ectonucleotide pyrophosphatase phosphodiesterase (npp1) | |
| US10456451B2 (en) | Protease-resistant mutants of stromal cell derived factor-1 in the repair of tissue damage | |
| JP2017500316A (ja) | ストロマ細胞由来因子−1のプロテアーゼ耐性変異体を用いた、組織損傷を修復する方法 | |
| WO2012027170A1 (en) | Methods for repairing tissue damage using protease-resistant mutants of stromal cell derived factor-1 | |
| HK1196944A (en) | Methods for repairing tissue damage using protease-resistant mutants of stromal cell derived factor-1 | |
| HK1196944B (en) | Methods for repairing tissue damage using protease-resistant mutants of stromal cell derived factor-1 | |
| HK1223556B (zh) | Il-22二聚体在制备用於治疗胰腺炎的药物中的用途 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20150205 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20150205 |
|
| RD04 | Notification of resignation of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7424 Effective date: 20150325 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20151130 |
|
| RD03 | Notification of appointment of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7423 Effective date: 20160204 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20160215 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20160204 |
|
| RD04 | Notification of resignation of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7424 Effective date: 20160204 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20160927 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20170127 |
|
| A911 | Transfer to examiner for re-examination before appeal (zenchi) |
Free format text: JAPANESE INTERMEDIATE CODE: A911 Effective date: 20170309 |
|
| TRDD | Decision of grant or rejection written | ||
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20170418 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20170512 |
|
| R150 | Certificate of patent or registration of utility model |
Ref document number: 6145089 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| LAPS | Cancellation because of no payment of annual fees |